Gene silencing of two acetylcholinesterases reveals their cholinergic and non-cholinergic functions in Rhopalosiphum padi and Sitobion avenae

BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. RESULTS The transcript levels of the...

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Published in	Pest management science Vol. 71; no. 4; pp. 523 - 530
Main Authors	Xiao, Da, Lu, Yan-Hui, Shang, Qing-Li, Song, Dun-Lun, Gao, Xi-Wu
Format	Journal Article
Language	English
Published	Chichester, UK John Wiley & Sons, Ltd 01.04.2015 Wiley Subscription Services, Inc
Subjects	acetylcholinesterase Acetylcholinesterase - genetics Acetylcholinesterase - metabolism Animals Aphididae Aphids - drug effects Aphids - genetics Aphids - metabolism Bioassays Carbamates - pharmacology Cholinesterase Inhibitors - metabolism Enzymes gene function Gene Silencing Genes Insect Proteins - genetics Insect Proteins - metabolism Insecticides - pharmacology Insects Malathion - pharmacology Pest control Pyrimidines - pharmacology Rhopalosiphum padi RNA interference Sitobion avenae Species Specificity Toxicology acetylcholinesterase gene function RNA interference Rhopalosiphum padi Sitobion avenae
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Abstract	BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. RESULTS The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae. However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2. Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae, whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. CONCLUSIONS These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae. It also plays a non‐cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1. © 2014 Society of Chemical Industry
AbstractList	Abstract BACKGROUD The function of acetylcholinesterase ( AChE ) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine ( ACh ) in the synaptic cleft, and thus it is an effective target for organophosphate ( OP ) and carbamate ( CB ) insecticides. RESULTS The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae . However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2 . Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae , whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. CONCLUSIONS These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae . It also plays a non‐cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1 . © 2014 Society of Chemical Industry BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. RESULTS The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae. However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2. Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae, whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. CONCLUSIONS These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae. It also plays a non‐cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1. © 2014 Society of Chemical Industry BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. RESULTS The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae . However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2 . Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae , whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. CONCLUSIONS These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae . It also plays a non-cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1. copyright 2014 Society of Chemical Industry The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae. However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2. Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae, whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae. It also plays a non-cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1. The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic cleft, and thus it is an effective target for organophosphate (OP) and carbamate (CB) insecticides. The transcript levels of the four Ace genes were dramatically suppressed by injection of their respective dsRNA in Rhopalosiphum padi and Sitobion avenae. However, the AChE activity changes in the Ace1 knockdown aphids were consistent with the significant transcript level changes of Ace1 genes in these aphids, but not for Ace2. Bioassay results indicated that the suppression of RpAce1 increased its susceptibilities to pirimicarb and malathion, and SaAce1 silencing also increased susceptibility to pirimicarb in S. avenae, whereas the knockdowns of RpAce2 and SaAce2 had a slight effect on their susceptibilities. The knockdown of Ace1 genes also caused significant reductions in fecundity in the aphids of their parental generation. These results suggest that AChE1 is a predominant cholinergic enzyme and is the target of anticholinesterase insecticides in both R. padi and S. avenae. It also plays a non-cholinergic role in fecundity of these aphids. AChE2 may also be important for the toxicological function, although its importance appeared to be lower than that of AChE1.
Author	Song, Dun-Lun Lu, Yan-Hui Xiao, Da Gao, Xi-Wu Shang, Qing-Li
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Cites_doi	10.1111/j.0962-1075.2004.00513.x 10.1016/j.bbrc.2006.12.088 10.1111/j.1742-4658.2007.06237.x 10.1371/journal.pone.0004349 10.1042/bj3590175 10.1673/031.013.0901 10.1016/0006-2952(75)90443-8 10.1098/rspb.2002.2122 10.1073/pnas.0508866103 10.1016/S0006-291X(03)01101-X 10.1038/35067589 10.1093/jmedent/43.5.878 10.1016/j.pestbp.2008.11.007 10.1016/j.jinsphys.2008.12.005 10.1016/j.coph.2005.01.014 10.1016/j.pestbp.2006.09.005 10.1016/j.pestbp.2012.01.004 10.1046/j.1365-2583.1998.72055.x 10.1016/0003-2697(76)90527-3 10.1016/j.bbrc.2008.11.046 10.1016/j.cbi.2008.03.018 10.1007/BF00554410 10.1111/j.1365-2583.2005.00576.x 10.1016/0006-2952(61)90145-9 10.1371/journal.pone.0032288 10.1016/j.pestbp.2005.12.002 10.1006/pest.1996.0064 10.1016/j.ibmb.2009.11.001 10.1002/j.1460-2075.1986.tb04591.x 10.1016/S0965-1748(01)00159-X 10.1093/molbev/msm025 10.1673/031.006.3801 10.1098/rspb.2006.3621 10.1158/0008-5472.CAN-04-0649 10.1371/journal.pgen.0030205 10.1017/S0007485309006725 10.3389/fnmol.2012.00040 10.1016/j.ibmb.2007.12.008 10.1186/1475-2875-8-70 10.1002/arch.21007 10.1038/423136b 10.1016/0301-0082(89)90031-2 10.1016/j.pestbp.2004.12.003 10.1111/j.1365-2583.2011.01081.x 10.1016/j.cbi.2010.03.034 10.1139/G05-104 10.1016/j.ibmb.2008.07.007 10.1038/srep00288 10.1186/1472-6750-7-63 10.1126/science.1091789
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Keywords	acetylcholinesterase gene function RNA interference Rhopalosiphum padi Sitobion avenae
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References	Osta MA, Christophides GK and Kafatos FC, Effects of mosquito genes on plasmodium development. Science 303:2030-2032 (2004). Lu YH, He YP and Gao XW, Comparative studies on acetylcholinesterase characteristics between the aphids, Sitobion avenae and Rhopalosiphum padi. J Insect Sci 13:9 (2013). Soreq H and Seidman S, Acetylcholinesterase - new roles for an old actor. Nat Rev Neurosci 2:294-302 (2001). Kono Y and Tomita T, Amino acid substitutions conferring insecticide insensitivity in Ace-paralogous acetylcholinesterase. Pestic Biochem Physiol 85:123-132 (2006). Bourguet D, Raymond M, Bisset J, Pasteur N and Arpagaus M, Duplication of the Ace.1 locus in Culex pipiens mosquitoes from the Caribbean. Biochem Genet 34:351-362 (1996). Hall LMC and Spierer P, The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader. EMBO J 5:2949-2954 (1986). Weill M, Lutfalla G, Mogensen K, Chandre F, Berthomieu A, Berticat C et al., Insecticide resistance in mosquito vectors. Nature 423:136-137 (2003). Gao XW, Introduction of Ellman procedure for assay of cholinesterases in crude enzymatic preparations modified by Gorun. Chin Bull Entomol 33:245-246 (1987). Weill M, Fort P, Berthomieu A, Dubois MP, Pasteur N and Raymond M, A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene Drosophila. Proc R Soc Lond B 269:2007-2016 (2002). Nabeshima T, Kozaki T, Tomita T and Kono Y, An amino acid substitution on the second acetylcholinesterase in the pirimicarb-resistant strains of the peach potato aphid, Myzus persicae. Biochem Biophys Res Commun 307:15-22 (2003). Lu YH and Gao XW, A method for mass culture of wheat aphids. Chin Bull Entomol 44:289-290 (2007). Toda S, Komazaki S, Tomita T and Kono Y, Two amino acid substitutions in acetylcholinesterase associated with pirimicarb and organophosphorous insecticide resistance in the cotton aphid, Aphis gossypii Glover (Homoptera: Aphididae). Insect Mol Biol 13:549-553 (2004). Pegan K, Matkovic U, Mars T, Mis K, Pirkmajer S, Brecelj J et al., Acetylcholinesterase is involved in apoptosis in the precursors of human muscle regeneration. Chem Biol Interact 187:96-100 (2010). Fournier D and Mutero A, Modification of acetylcholinesterase as a mechanism of resistance to insecticides. Comp Biochem Physiol 108C:19-31 (1994). Ellman GL, Courtney KD, Andres VJR and Featherstone RM, A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88-95 (1961). Jiang XJ, Qu MJ, Denholm I, Fang JC, Jiang WH and Han ZJ, Mutation in acetylcholinesterase 1 associated with triazophos resistance in rice stem borer, Chilo suppressalis (Lepidoptera: Pyralidae). Biochem Biophys Res Commun 378:269-272 (2009). Labbe P, Berthomieu A, Berticat C, Alout H, Raymond M, Lenormand T et al., Independent duplications of the acetylcholinesterase gene conferring insecticide resistance in the mosquito Culex pipiens. Mol Biol Evol 24:1056-1067 (2007). Togawa T, Dunn WA, Emmons AC, Nagao J and Willis JH, Developmental expression patterns of cuticular protein genes with the R&R Consensus from Anopheles gambiae. Insect Biochem Mol Biol 38:508-519 (2008). Pang YP, Singh SK, Gao Y, Lassiter TL, Mishra RK, Zhu KY et al., Selective and irreversible inhibitors of aphid acetylcholinesterases: steps toward human-safe insecticides. PLoS ONE 4:e4349 (2009). Park SE, Kim ND and Yoo YH, Acetylcholinesterase plays a pivotal role in apoptosome formation. Cancer Res 64:2652-2655 (2004). Arakane Y, Muthukrishnan S, Kramer KJ, Specht CA, Tomoyasu Y, Lorenzen MD et al., The Tribolium chitin synthase genes TcCHS1 and TcCHS2 are specialized for synthesis of epidermal cuticle and midgut peritrophic matrix. Insect Mol Biol 14:453-463 (2005). Alon M, Alon F, Nauen R and Morin S, Organophosphates' resistance in the B-biotype of Bemisia tabaci (Hemiptera: Aleyrodidae) is associated with a point mutation in an ace1-type acetylcholinesterase and overexpression of carboxylesterase. Insect Biochem Mol Biol 38:940-949 (2008). Zhou XG, Oi FM and Scharf ME, Social exploitation of hexamerin: RNAi reveals a major caste-regulatory factor in termites. Proc Natl Acad Sci USA 103:4499-4504 (2006). Paraoanu LE and Layer PG, Acetylcholinesterase in cell adhesion, neurite growth and network formation. FEBS J 275:618-624 (2008). Revuelta L, Piulachs MD, Bellés X, Castañera P, Ortego F, Díaz-Ruíz JR et al., RNAi of ace1 and ace2 in Blattella germanica reveals their differential contribution to acetylcholinesterase activity and sensitivity to insecticides. Insect Biochem Mol Biol 39:913-919 (2009). Gao JR, Kambhampati S and Zhu KY, Molecular cloning and characterization of a greenbug (Schizaphis graminum) cDNA encoding acetylcholinesterase possibly evolved from a duplicate gene lineage. Insect Biochem Mol Biol 32:765-775 (2002). Hui XM, Yang LW, He GL, Yang QP, Han ZJ and Li F, RNA interference of ace1 and ace2 in Chilo suppressalis reveals their different contributions to motor ability and larval growth. Insect Mol Biol 20:507-518 (2011). Silman I and Sussman JL, Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology. Curr Opin Pharmacol 5:293-302 (2005). Lu YH, Park Y, Gao XW, Zhang X, Yao JX, Pang YP et al., Cholinergic and non-cholinergic functions of two acetylcholinesterase genes revealed by gene-silencing in Tribolium castaneum. Sci Rep 2:288 (2012). Li BL, Chen W, Liu L, Zhang XC, Bao YY, Chen JA et al., Molecular characterization of two acetylcholinesterase genes from the brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae). Pestic Biochem Physiol 102:198-203 (2012). Labbé P, Berticat C, Berthomieu A, Unal S, Bernard C, Weill M et al., Forty years of erratic insecticide resistance evolution in the mosquito Culex pipiens. PLoS Genet 3:e205 (2007). Toutant JP, Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Prog Neurobiol 32:423-446 (1989). Walsh SB, Dolden TA, Moores GD, Kristensen M, Lewis T, Devonshire AL et al., Identification and characterization of mutations in housefly (Musca domestica) acetylcholinesterase involved in insecticide resistance. Biochem J 359:175-181 (2001). Seino A, Kazuma T, Tan AJ, Tanaka H, Kono Y, Mita K et al., Analysis of two acetylcholinesterase genes in Bombyx mori. Pestic Biochem Physiol 88:92-101 (2007). Lee DW, Choi JY, Kim WT, Je YH, Song JT, Chung BK et al., Mutations of acetylcholinesterase 1 contribute to prothiofos-resistance in Plutella xylostella (L.). Biochem Biophys Res Commun 353:591-597 (2007). Mutti NS, Park Y, Reese JC and Reeck GR, RNAi knockdown of a salivary transcript leading to lethality in the pea aphid, Acyrthosiphon pisum. J Insect Sci 6:38 (2006). Djogbénou L, Labbé P, Chandre F, Pasteur N and Weill M, Ace-1 duplication in Anopheles gambiae: a challenge for malaria control. Malaria J 8:70 (2009). Lu YH, Pang YP, Park Y, Gao XW, Yao JX, Zhang X et al., Genome organization, phylogenies, expression patterns, and three-dimensional protein models of two acetylcholinesterase genes from the red flour beetle. PloS ONE 7:e32288 (2012). Baek JH, Kim JI, Lee DW, Chung BK, Miyata T and Lee SH, Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella. Pestic Biochem Physiol 81:164-175 (2005). Djogbénou L, Chandre F, Berthomieu A, Dabire R, Koffi A, Alout H et al., Evidence of introgression of the ace-1R mutation and of the ace-1 duplication in West African Anopheles gambiae s. s. PLoS ONE 3:e2172 (2008). Jaubert-Possamai S, Le Trionnaire G, Bonhomme J, Christophides GK, Rispe C and Tagu D, Gene knockdown by RNAi in the pea aphid Acyrthosiphon pisum. BMC Biotechnol 7:63 (2007). Cui F, Raymond M, Berthomieu A, Alout H, Weill M and Qiao Cl, Recent emergence of insensitive acetylcholinesterase in Chinese populations of the mosquito Culex pipiens (Diptera: Culicidae). J Med Entomol 43:878-883 (2006). He GL, Sun Y and Li F, RNA interference of two acetylcholinesterase genes in Plutella xylostella reveals their different function. Arch Insect Biochem Physiol 79:75-86 (2012). Moores GD, Gao XW, Denholm I and Devonshire AL, Characterisation of insensitive acetylcholinesterase in insecticide-resistant cotton aphids, Aphis gossypii Glover (Homoptera: Aphididae). Pestic Biochem Physiol 56:102-110 (1996). Zhou X and Xia Y, Cloning of an acetylcholinesterase gene in Locusta migratoria manilensis related to organophosphate insecticide resistance. Pestic Biochem Physiol 93:77-84 (2009). Malcolm CA, Bourguet D, Ascolillo A, Rooker SJ, Garvey CF, Hall LMC et al., A sex-linked Ace gene, not linked to insensitive acetylcholinesterase-mediated insecticide resistance in Culex pipiens. Insect Mol Biol 7:107-120 (1998). Alout H and Weill M, Amino-acid substitutions in acetylcholinesterase 1 involved in insecticide resistance in mosquitoes. Chem Biol Interact 175:138-141 (2008). Bradford MM, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254 (1976). Chen MH and Han ZJ, Cloning and sequence analysis of 2 different acetylcholinesterase genes in Rhopalosiphum padi and Sitobion avenae. Genome 49:239-243 (2006). Lu YH and Gao XW, Multiple mechanisms responsible for differential susceptibilities of Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) to pirimicarb. Bull Entomol Res 99:611-617 (2009). Zhang XJ and Greenberg DS, Acetylcholinesterase involvement in apoptosis. Front Mol Neurosci 5:40 (2012). Smissaert HR, el Hamid FM and Overmeer WP, The minimum acetycholinesterase (AChE) fraction compatible with life derived by aid of a simple model explaining the degree of dominance of resistance to inhibitors in AChE 'mutants'. Biochem Pharmacol 24:1043-1047 (1975). Kumar M, Gupta GP and Rajam MV, Silencing of acetylcholinesterase gene of Helicoverpa armigera by siRNA affects larval grow 1987; 33 2004; 64 1994; 108C 2008; 38 2010; 187 2008; 3 1996; 34 2009; 55 2009; 99 1989; 32 2013; 13 1961; 7 2009; 93 1976; 72 1986; 5 2011; 20 2002; 269 2007; 7 2007; 3 2008; 275 2007; 24 2004; 303 2012; 102 2002; 32 2006; 273 2006; 6 2005; 81 2012; 79 2009; 378 1996; 56 2003; 307 2006; 85 2012; 2 2006; 43 2006; 49 2007; 353 2004; 13 2005; 5 1975; 24 2009; 8 2001; 2 2009; 4 2003; 423 1998; 7 2012; 7 2007; 88 2007; 44 2008; 175 2012; 5 2001; 359 2006; 103 2009; 39 2005; 14 e_1_2_6_51_1 e_1_2_6_53_1 e_1_2_6_32_1 e_1_2_6_30_1 Gao XW (e_1_2_6_44_1) 1987; 33 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_36_1 e_1_2_6_11_1 e_1_2_6_34_1 e_1_2_6_17_1 e_1_2_6_55_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_43_1 e_1_2_6_20_1 e_1_2_6_41_1 Djogbénou L (e_1_2_6_28_1) 2008; 3 e_1_2_6_9_1 e_1_2_6_5_1 e_1_2_6_7_1 e_1_2_6_24_1 e_1_2_6_49_1 e_1_2_6_22_1 e_1_2_6_45_1 e_1_2_6_26_1 e_1_2_6_47_1 e_1_2_6_52_1 e_1_2_6_54_1 e_1_2_6_10_1 e_1_2_6_31_1 Lu YH (e_1_2_6_40_1) 2007; 44 e_1_2_6_50_1 Fournier D (e_1_2_6_3_1) 1994; 108 Cui F (e_1_2_6_23_1) 2006; 43 e_1_2_6_14_1 e_1_2_6_35_1 e_1_2_6_12_1 e_1_2_6_33_1 e_1_2_6_18_1 e_1_2_6_39_1 e_1_2_6_16_1 e_1_2_6_37_1 e_1_2_6_42_1 e_1_2_6_21_1 e_1_2_6_8_1 e_1_2_6_4_1 e_1_2_6_6_1 e_1_2_6_25_1 e_1_2_6_48_1 e_1_2_6_2_1 e_1_2_6_29_1 e_1_2_6_27_1 e_1_2_6_46_1
References_xml	– volume: 4 start-page: e4349 year: 2009 article-title: Selective and irreversible inhibitors of aphid acetylcholinesterases: steps toward human‐safe insecticides publication-title: PLoS ONE – volume: 3 issue: e2172 year: 2008 article-title: Evidence of introgression of the mutation and of the duplication in West African publication-title: PLoS ONE – volume: 303 start-page: 2030 year: 2004 end-page: 2032 article-title: Effects of mosquito genes on plasmodium development publication-title: Science – volume: 7 start-page: 88 year: 1961 end-page: 95 article-title: A new and rapid colorimetric determination of acetylcholinesterase activity publication-title: Biochem Pharmacol – volume: 32 start-page: 765 year: 2002 end-page: 775 article-title: Molecular cloning and characterization of a greenbug ( ) cDNA encoding acetylcholinesterase possibly evolved from a duplicate gene lineage publication-title: Insect Biochem Mol Biol – volume: 20 start-page: 507 year: 2011 end-page: 518 article-title: RNA interference of 1 and 2 in reveals their different contributions to motor ability and larval growth publication-title: Insect Mol Biol – volume: 7 start-page: e32288 year: 2012 article-title: Genome organization, phylogenies, expression patterns, and three‐dimensional protein models of two acetylcholinesterase genes from the red flour beetle publication-title: PloS ONE – volume: 7 start-page: 107 year: 1998 end-page: 120 article-title: A sex‐linked gene, not linked to insensitive acetylcholinesterase‐mediated insecticide resistance in publication-title: Insect Mol Biol – volume: 99 start-page: 611 year: 2009 end-page: 617 article-title: Multiple mechanisms responsible for differential susceptibilities of (Fabricius) and (Linnaeus) to pirimicarb publication-title: Bull Entomol Res – volume: 6 start-page: 38 year: 2006 article-title: RNAi knockdown of a salivary transcript leading to lethality in the pea aphid, publication-title: J Insect Sci – volume: 3 start-page: e205 year: 2007 article-title: Forty years of erratic insecticide resistance evolution in the mosquito publication-title: PLoS Genet – volume: 2 start-page: 294 year: 2001 end-page: 302 article-title: Acetylcholinesterase – new roles for an old actor publication-title: Nat Rev Neurosci – volume: 108C start-page: 19 year: 1994 end-page: 31 article-title: Modification of acetylcholinesterase as a mechanism of resistance to insecticides publication-title: Comp Biochem Physiol – volume: 5 start-page: 40 year: 2012 article-title: Acetylcholinesterase involvement in apoptosis publication-title: Front Mol Neurosci – volume: 7 start-page: 63 year: 2007 article-title: Gene knockdown by RNAi in the pea aphid publication-title: BMC Biotechnol – volume: 378 start-page: 269 year: 2009 end-page: 272 article-title: Mutation in acetylcholinesterase 1 associated with triazophos resistance in rice stem borer, (Lepidoptera: Pyralidae) publication-title: Biochem Biophys Res Commun – volume: 307 start-page: 15 year: 2003 end-page: 22 article-title: An amino acid substitution on the second acetylcholinesterase in the pirimicarb‐resistant strains of the peach potato aphid publication-title: Myzus persicae. Biochem Biophys Res Commun – volume: 24 start-page: 1043 year: 1975 end-page: 1047 article-title: The minimum acetycholinesterase (AChE) fraction compatible with life derived by aid of a simple model explaining the degree of dominance of resistance to inhibitors in AChE ‘mutants’ publication-title: Biochem Pharmacol – volume: 34 start-page: 351 year: 1996 end-page: 362 article-title: Duplication of the locus in mosquitoes from the Caribbean publication-title: Biochem Genet – volume: 44 start-page: 289 year: 2007 end-page: 290 article-title: A method for mass culture of wheat aphids publication-title: Chin Bull Entomol – volume: 55 start-page: 273 year: 2009 end-page: 278 article-title: Silencing of acetylcholinesterase gene of by siRNA affects larval growth and its life cycle publication-title: J Insect Physiol – volume: 39 start-page: 913 year: 2009 end-page: 919 article-title: RNAi of and in reveals their differential contribution to acetylcholinesterase activity and sensitivity to insecticides publication-title: Insect Biochem Mol Biol – volume: 175 start-page: 138 year: 2008 end-page: 141 article-title: Amino‐acid substitutions in acetylcholinesterase 1 involved in insecticide resistance in mosquitoes publication-title: Chem Biol Interact – volume: 88 start-page: 92 year: 2007 end-page: 101 article-title: Analysis of two acetylcholinesterase genes in publication-title: Pestic Biochem Physiol – volume: 273 start-page: 2595 year: 2006 end-page: 2604 article-title: Acetylcholinesterase genes within the Diptera: takeover and loss in true flies publication-title: Proc R Soc Lond B – volume: 423 start-page: 136 year: 2003 end-page: 137 article-title: Insecticide resistance in mosquito vectors publication-title: Nature – volume: 33 start-page: 245 year: 1987 end-page: 246 article-title: Introduction of Ellman procedure for assay of cholinesterases in crude enzymatic preparations modified by Gorun publication-title: Chin Bull Entomol – volume: 72 start-page: 248 year: 1976 end-page: 254 article-title: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding publication-title: Anal Biochem – volume: 187 start-page: 96 year: 2010 end-page: 100 article-title: Acetylcholinesterase is involved in apoptosis in the precursors of human muscle regeneration publication-title: Chem Biol Interact – volume: 269 start-page: 2007 year: 2002 end-page: 2016 article-title: A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non‐homologous to the gene publication-title: Proc R Soc Lond B – volume: 85 start-page: 123 year: 2006 end-page: 132 article-title: Amino acid substitutions conferring insecticide insensitivity in ‐paralogous acetylcholinesterase publication-title: Pestic Biochem Physiol – volume: 79 start-page: 75 year: 2012 end-page: 86 article-title: RNA interference of two acetylcholinesterase genes in reveals their different function publication-title: Arch Insect Biochem Physiol – volume: 49 start-page: 239 year: 2006 end-page: 243 article-title: Cloning and sequence analysis of 2 different acetylcholinesterase genes in and publication-title: Genome – volume: 14 start-page: 453 year: 2005 end-page: 463 article-title: The genes and are specialized for synthesis of epidermal cuticle and midgut peritrophic matrix publication-title: Insect Mol Biol – volume: 275 start-page: 618 year: 2008 end-page: 624 article-title: Acetylcholinesterase in cell adhesion, neurite growth and network formation publication-title: FEBS J – volume: 43 start-page: 878 year: 2006 end-page: 883 article-title: Recent emergence of insensitive acetylcholinesterase in Chinese populations of the mosquito (Diptera: Culicidae) publication-title: J Med Entomol – volume: 102 start-page: 198 year: 2012 end-page: 203 article-title: Molecular characterization of two acetylcholinesterase genes from the brown planthopper, (Hemiptera: Delphacidae) publication-title: Pestic Biochem Physiol – volume: 64 start-page: 2652 year: 2004 end-page: 2655 article-title: Acetylcholinesterase plays a pivotal role in apoptosome formation publication-title: Cancer Res – volume: 13 start-page: 9 year: 2013 article-title: Comparative studies on acetylcholinesterase characteristics between the aphids, and publication-title: J Insect Sci – volume: 13 start-page: 549 year: 2004 end-page: 553 article-title: Two amino acid substitutions in acetylcholinesterase associated with pirimicarb and organophosphorous insecticide resistance in the cotton aphid, Glover (Homoptera: Aphididae) publication-title: Insect Mol Biol – volume: 93 start-page: 77 year: 2009 end-page: 84 article-title: Cloning of an acetylcholinesterase gene in related to organophosphate insecticide resistance publication-title: Pestic Biochem Physiol – volume: 353 start-page: 591 year: 2007 end-page: 597 article-title: Mutations of acetylcholinesterase 1 contribute to prothiofos‐resistance in (L.) publication-title: Biochem Biophys Res Commun – volume: 24 start-page: 1056 year: 2007 end-page: 1067 article-title: Independent duplications of the acetylcholinesterase gene conferring insecticide resistance in the mosquito publication-title: Mol Biol Evol – volume: 56 start-page: 102 year: 1996 end-page: 110 article-title: Characterisation of insensitive acetylcholinesterase in insecticide‐resistant cotton aphids, Glover (Homoptera: Aphididae) publication-title: Pestic Biochem Physiol – volume: 359 start-page: 175 year: 2001 end-page: 181 article-title: Identification and characterization of mutations in housefly ( ) acetylcholinesterase involved in insecticide resistance publication-title: Biochem J – volume: 2 start-page: 288 year: 2012 article-title: Cholinergic and non‐cholinergic functions of two acetylcholinesterase genes revealed by gene‐silencing in publication-title: Sci Rep – volume: 5 start-page: 293 year: 2005 end-page: 302 article-title: Acetylcholinesterase: ‘classical’ and ‘non‐classical’ functions and pharmacology publication-title: Curr Opin Pharmacol – volume: 38 start-page: 940 year: 2008 end-page: 949 article-title: Organophosphates' resistance in the B‐biotype of (Hemiptera: Aleyrodidae) is associated with a point mutation in an ‐type acetylcholinesterase and overexpression of carboxylesterase publication-title: Insect Biochem Mol Biol – volume: 103 start-page: 4499 year: 2006 end-page: 4504 article-title: Social exploitation of hexamerin: RNAi reveals a major caste‐regulatory factor in termites publication-title: Proc Natl Acad Sci USA – volume: 8 start-page: 70 year: 2009 article-title: duplication in : a challenge for malaria control publication-title: Malaria J – volume: 32 start-page: 423 year: 1989 end-page: 446 article-title: Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms publication-title: Prog Neurobiol – volume: 5 start-page: 2949 year: 1986 end-page: 2954 article-title: The locus of : structural gene for acetylcholinesterase with an unusual 5′ leader publication-title: EMBO J – volume: 81 start-page: 164 year: 2005 end-page: 175 article-title: Identification and characterization of ‐type acetylcholinesterase likely associated with organophosphate resistance in publication-title: Pestic Biochem Physiol – volume: 38 start-page: 508 year: 2008 end-page: 519 article-title: Developmental expression patterns of cuticular protein genes with the R&R Consensus from publication-title: Insect Biochem Mol Biol – ident: e_1_2_6_21_1 doi: 10.1111/j.0962-1075.2004.00513.x – volume: 44 start-page: 289 year: 2007 ident: e_1_2_6_40_1 article-title: A method for mass culture of wheat aphids publication-title: Chin Bull Entomol contributor: fullname: Lu YH – ident: e_1_2_6_22_1 doi: 10.1016/j.bbrc.2006.12.088 – ident: e_1_2_6_32_1 doi: 10.1111/j.1742-4658.2007.06237.x – ident: e_1_2_6_53_1 doi: 10.1371/journal.pone.0004349 – ident: e_1_2_6_30_1 doi: 10.1042/bj3590175 – ident: e_1_2_6_39_1 doi: 10.1673/031.013.0901 – ident: e_1_2_6_54_1 doi: 10.1016/0006-2952(75)90443-8 – ident: e_1_2_6_4_1 doi: 10.1098/rspb.2002.2122 – ident: e_1_2_6_50_1 doi: 10.1073/pnas.0508866103 – ident: e_1_2_6_11_1 doi: 10.1016/S0006-291X(03)01101-X – ident: e_1_2_6_51_1 doi: 10.1038/35067589 – volume: 43 start-page: 878 year: 2006 ident: e_1_2_6_23_1 article-title: Recent emergence of insensitive acetylcholinesterase in Chinese populations of the mosquito Culex pipiens (Diptera: Culicidae) publication-title: J Med Entomol doi: 10.1093/jmedent/43.5.878 contributor: fullname: Cui F – ident: e_1_2_6_55_1 doi: 10.1016/j.pestbp.2008.11.007 – ident: e_1_2_6_35_1 doi: 10.1016/j.jinsphys.2008.12.005 – ident: e_1_2_6_52_1 doi: 10.1016/j.coph.2005.01.014 – volume: 33 start-page: 245 year: 1987 ident: e_1_2_6_44_1 article-title: Introduction of Ellman procedure for assay of cholinesterases in crude enzymatic preparations modified by Gorun publication-title: Chin Bull Entomol contributor: fullname: Gao XW – ident: e_1_2_6_14_1 doi: 10.1016/j.pestbp.2006.09.005 – ident: e_1_2_6_17_1 doi: 10.1016/j.pestbp.2012.01.004 – ident: e_1_2_6_20_1 doi: 10.1046/j.1365-2583.1998.72055.x – ident: e_1_2_6_45_1 doi: 10.1016/0003-2697(76)90527-3 – ident: e_1_2_6_16_1 doi: 10.1016/j.bbrc.2008.11.046 – ident: e_1_2_6_24_1 doi: 10.1016/j.cbi.2008.03.018 – ident: e_1_2_6_25_1 doi: 10.1007/BF00554410 – ident: e_1_2_6_49_1 doi: 10.1111/j.1365-2583.2005.00576.x – ident: e_1_2_6_43_1 doi: 10.1016/0006-2952(61)90145-9 – ident: e_1_2_6_10_1 doi: 10.1371/journal.pone.0032288 – ident: e_1_2_6_9_1 doi: 10.1016/j.pestbp.2005.12.002 – ident: e_1_2_6_42_1 doi: 10.1006/pest.1996.0064 – ident: e_1_2_6_18_1 doi: 10.1016/j.ibmb.2009.11.001 – ident: e_1_2_6_6_1 doi: 10.1002/j.1460-2075.1986.tb04591.x – ident: e_1_2_6_7_1 doi: 10.1016/S0965-1748(01)00159-X – ident: e_1_2_6_26_1 doi: 10.1093/molbev/msm025 – ident: e_1_2_6_41_1 doi: 10.1673/031.006.3801 – ident: e_1_2_6_8_1 doi: 10.1098/rspb.2006.3621 – ident: e_1_2_6_31_1 doi: 10.1158/0008-5472.CAN-04-0649 – ident: e_1_2_6_27_1 doi: 10.1371/journal.pgen.0030205 – ident: e_1_2_6_38_1 doi: 10.1017/S0007485309006725 – ident: e_1_2_6_34_1 doi: 10.3389/fnmol.2012.00040 – volume: 108 start-page: 19 year: 1994 ident: e_1_2_6_3_1 article-title: Modification of acetylcholinesterase as a mechanism of resistance to insecticides publication-title: Comp Biochem Physiol contributor: fullname: Fournier D – ident: e_1_2_6_46_1 doi: 10.1016/j.ibmb.2007.12.008 – ident: e_1_2_6_29_1 doi: 10.1186/1475-2875-8-70 – ident: e_1_2_6_37_1 doi: 10.1002/arch.21007 – ident: e_1_2_6_5_1 doi: 10.1038/423136b – ident: e_1_2_6_2_1 doi: 10.1016/0301-0082(89)90031-2 – ident: e_1_2_6_12_1 doi: 10.1016/j.pestbp.2004.12.003 – ident: e_1_2_6_36_1 doi: 10.1111/j.1365-2583.2011.01081.x – ident: e_1_2_6_33_1 doi: 10.1016/j.cbi.2010.03.034 – volume: 3 issue: 2172 year: 2008 ident: e_1_2_6_28_1 article-title: Evidence of introgression of the ace‐1R mutation and of the ace‐1 duplication in West African Anopheles gambiae s. s publication-title: PLoS ONE contributor: fullname: Djogbénou L – ident: e_1_2_6_13_1 doi: 10.1139/G05-104 – ident: e_1_2_6_15_1 doi: 10.1016/j.ibmb.2008.07.007 – ident: e_1_2_6_19_1 doi: 10.1038/srep00288 – ident: e_1_2_6_47_1 doi: 10.1186/1472-6750-7-63 – ident: e_1_2_6_48_1 doi: 10.1126/science.1091789
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Snippet	BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the... The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the synaptic... Abstract BACKGROUD The function of acetylcholinesterase ( AChE ) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine ( ACh... BACKGROUD The function of acetylcholinesterase (AChE) is to terminate synaptic transmission by hydrolysing the neurotransmitter acetylcholine (ACh) in the...
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SubjectTerms	acetylcholinesterase Acetylcholinesterase - genetics Acetylcholinesterase - metabolism Animals Aphididae Aphids - drug effects Aphids - genetics Aphids - metabolism Bioassays Carbamates - pharmacology Cholinesterase Inhibitors - metabolism Enzymes gene function Gene Silencing Genes Insect Proteins - genetics Insect Proteins - metabolism Insecticides - pharmacology Insects Malathion - pharmacology Pest control Pyrimidines - pharmacology Rhopalosiphum padi RNA interference Sitobion avenae Species Specificity Toxicology
Title	Gene silencing of two acetylcholinesterases reveals their cholinergic and non-cholinergic functions in Rhopalosiphum padi and Sitobion avenae
URI	https://api.istex.fr/ark:/67375/WNG-HRR3GBCM-P/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fps.3800 https://www.ncbi.nlm.nih.gov/pubmed/24729410 https://www.proquest.com/docview/1664814122/abstract/ https://search.proquest.com/docview/1668246133
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